Structure of mammalian steroid receptors: evolving concepts and methodological developments.
Structure of mammalian steroid receptors: evolving concepts and methodological developments.
复制标题
哺乳动物类固醇受体的结构:概念的演变和方法的发展。
DOI:
10.1146/annurev.ph.46.030184.000503
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发表时间:
1984
影响因子:
18.2
通讯作者:
Stevens,J
中科院分区:
文献类型:
--
作者:
Sherman,MR;Stevens,J
Despite much work and significant progress on the stabilization, purification, and structural analysis of steroid receptors extracted from mammalian tissues, the native state still remains largely unknown. Receptors for a single class of steroids from the same tissue have been detected in various molecular forms and at least three functional states. In this review, these states are referred to as the untransformed, transformed, and inactive states. They are distinguished by differences in the affinity of the receptor for steroids and in the affinity of the steroid-receptor complex for nuclei, DNA, and ionic resins. The untransformed steroid-receptor complexes are detected in cytoplasmic extracts (cytosols) of cells or tissues that were incubated with steroid in the cold, or in cytosols incubated with steroid at low temperature and low ionic strength. These complexes are characterized by low affinity for nuclei, chromatin, DNA, or anionic resins, such as DNA-cellulose or ATP-agarose, and high affinity for cationic resins, such as DEAE-cellulose or DEAE-agarose [reviewed in (15, 31, 63, 92)]. Transformation, defined as the acquisition of high affinity for nuclei, DNA, and anionic resins, is effected by warming cells that were incubated in the cold with steroid (68, 69, 123a) or by various manipulations of steroid-containing cytosols, such as prolonged storage, dilution, gel